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Hopkins researchers put proteins right where they want them
Date:4/14/2010

fferent locations such as Golgi bodies and mitrochondria, much less what happens when Ras is activated simultaneously at any combination of these and other organelles.

Working with live human HeLa cells and Ras under a microscope, the team used a dimerization probe consisting of a special small molecule that simultaneously attracts two proteins that wouldn't normally have an affinity for each other and binds them together. In this system, one of the partner proteins is anchored to an organelle and the other is free floating inside the cell. Adding a chemical dimerizer induces the free protein to join the tethered one.

Using scissor-like enzymes, the team sliced and diced the DNA of the paired proteins to change the molecular address of its destination. They cut out the "mailing address" known as a targeting sequence that formerly delivered the protein unit to the plasma membrane and replaced it with new addresses (targeting sequences) that shipped it instead to specific organelles.

"We were able to manipulate protein activities in situ and very rapidly on each individual organelle," Inoue said. "Ultimately, this will help us to better understand protein function at these critical cellular components."


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Contact: Maryalice Yakutchik
myakutc1@jhmi.edu
443-287-2251
Johns Hopkins Medical Institutions
Source:Eurekalert  

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